7B58
X-ray crystal structure of Sporosarcina pasteurii urease inhibited by Ag(PEt3)Cl determined at 1.72 Angstroms
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| AAA | 0005737 | cellular_component | cytoplasm |
| AAA | 0009039 | molecular_function | urease activity |
| AAA | 0016151 | molecular_function | nickel cation binding |
| AAA | 0016787 | molecular_function | hydrolase activity |
| AAA | 0019627 | biological_process | urea metabolic process |
| AAA | 0043419 | biological_process | urea catabolic process |
| BBB | 0005737 | cellular_component | cytoplasm |
| BBB | 0009039 | molecular_function | urease activity |
| BBB | 0016787 | molecular_function | hydrolase activity |
| BBB | 0035550 | cellular_component | urease complex |
| BBB | 0043419 | biological_process | urea catabolic process |
| CCC | 0005737 | cellular_component | cytoplasm |
| CCC | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
| CCC | 0009039 | molecular_function | urease activity |
| CCC | 0016151 | molecular_function | nickel cation binding |
| CCC | 0016787 | molecular_function | hydrolase activity |
| CCC | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| CCC | 0019627 | biological_process | urea metabolic process |
| CCC | 0043419 | biological_process | urea catabolic process |
| CCC | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305 |
| Chain | Residue | Details |
| CCC | HIS324 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 |
| Chain | Residue | Details |
| CCC | ALA364 | |
| CCC | VAL138 | |
| CCC | VAL276 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30969470 |
| Chain | Residue | Details |
| CCC | THR171 | |
| CCC | GLU223 | |
| CCC | SER250 | |
| CCC | MET367 | |
| CCC | PHE140 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231 |
| Chain | Residue | Details |
| CCC | ILE221 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10368287, ECO:0000269|PubMed:10766443, ECO:0000269|PubMed:11713685, ECO:0000269|PubMed:15038715, ECO:0000269|PubMed:30969470, ECO:0000269|DOI:10.1007/s007750050231, ECO:0007744|PDB:1IE7, ECO:0007744|PDB:1S3T, ECO:0007744|PDB:1UBP, ECO:0007744|PDB:2UBP, ECO:0007744|PDB:4UBP |
| Chain | Residue | Details |
| CCC | ILE221 |
